4buo: Difference between revisions

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 <StructureSection load='4buo' size='340' side='right'caption='[[4buo]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4buo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4buo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zev|3zev]], [[4bv0|4bv0]], [[4bwb|4bwb]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4buo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4buo OCA], [https://pdbe.org/4buo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4buo RCSB], [https://www.ebi.ac.uk/pdbsum/4buo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4buo ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4buo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4buo OCA], [http://pdbe.org/4buo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4buo RCSB], [http://www.ebi.ac.uk/pdbsum/4buo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4buo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NTR1_RAT NTR1_RAT]] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. [[http://www.uniprot.org/uniprot/NEUT_RAT NEUT_RAT]] Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle.
+[[https://www.uniprot.org/uniprot/NTR1_RAT NTR1_RAT]] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Crystallography has advanced our understanding of G protein-coupled receptors, but low expression levels and instability in solution have limited structural insights to very few selected members of this large protein family. Using neurotensin receptor 1 (NTR1) as a proof of principle, we show that two directed evolution technologies that we recently developed have the potential to overcome these problems. We purified three neurotensin-bound NTR1 variants from Escherichia coli and determined their X-ray structures at up to 2.75 A resolution using vapor diffusion crystallization experiments. A crystallized construct was pharmacologically characterized and exhibited ligand-dependent signaling, internalization, and wild-type-like agonist and antagonist affinities. Our structures are fully consistent with all biochemically defined ligand-contacting residues, and they represent an inactive NTR1 state at the cytosolic side. They exhibit significant differences to a previously determined NTR1 structure (Protein Data Bank ID code 4GRV) in the ligand-binding pocket and by the presence of the amphipathic helix 8. A comparison of helix 8 stability determinants between NTR1 and other crystallized G protein-coupled receptors suggests that the occupancy of the canonical position of the amphipathic helix is reduced to various extents in many receptors, and we have elucidated the sequence determinants for a stable helix 8. Our analysis also provides a structural rationale for the long-known effects of C-terminal palmitoylation reactions on G protein-coupled receptor signaling, receptor maturation, and desensitization.
-Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli.,Egloff P, Hillenbrand M, Klenk C, Batyuk A, Heine P, Balada S, Schlinkmann KM, Scott DJ, Schutz M, Pluckthun A Proc Natl Acad Sci U S A. 2014 Jan 22. PMID:24453215<ref>PMID:24453215</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4buo" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Neurotensin receptor|Neurotensin receptor]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Batyuk, A]]
+[[Category: Rattus norvegicus]]
-[[Category: Egloff, P]]
+[[Category: Batyuk A]]
-[[Category: Hillenbrand, M]]
+[[Category: Egloff P]]
-[[Category: Mittl, P]]
+[[Category: Hillenbrand M]]
-[[Category: Plueckthun, A]]
+[[Category: Mittl P]]
-[[Category: Schlinkmann, K M]]
+[[Category: Plueckthun A]]
-[[Category: G protein coupled receptor]]
+[[Category: Schlinkmann KM]]
-[[Category: Membrane protein]]
-[[Category: Signaling protein]]